##S And How Deletion Of Ykl Affects The Processes

##s And How Deletion Of Ykl Affects The Processes
Future steps Goal 1: 1.1: Super–resolution imaging of age–linked changes in actin cables and how deletion of Ykl affects those processes. We
optimized a method to isolate yeast of different replicative ages and will use 2 different modes of super–resolution imaging to further characterize
age–associated changes in the actin cytoskeleton. The resolution of conventional light microscopy (e.g. wide field and confocal) is diffraction limited,
which restricts the ability of microscope to distinguish between two objects separated by a lateral distance less than approximately half the wavelength
of excitation illumination. Structured illumination microscopy provides a 2–fold increase in axial (100 nm) and lateral (300 nm) resolution compared to
... Show more content on Helpwriting.net ...
1.3: Is the lifespan extension observed in yklв€† cells due to effects on actin cable stability? Here, the goal is to test whether reducing actin cable
stability prevents the lifespan extension produced by deletion of Ykl. We will reduce actin cable stability by mutating tropomyosin. There are two
tropomyosin isoforms in yeast, Tpm1 and Tpm2. Both isoforms localize to actin cables. However, Tpm1 stabilizes F–actin in actin cables. In contrast,
Tpm2 regulates RACF by inhibiting the binding of myosin to actin within actin cables. Previous studies in mammalian cells indicate that mutations in
the actin binding pocket of tropomyosin reduces their ability to bind to and stabilize F–actin. I will generate the same mutations in TPM1 and identify
conditions that reduces actin cable abundance to wild–type levels in yklв€† cells. Lastly, I will test whether restoring the wild
–type actin cable levels in
yklв€† cells prevents the lifespan extension originally seen in yklв€† cells. 1.4: Do interventions that promote actin cable function extend lifespan in
wild–type and yklв€† cells? We originally proposed to stabilize actin cables by treatment with the actin stabilizing drug jasplakinolide, or mild
overexpression of TPM1. Instead of relying on drugs or overexpression, we used CRISPR methods to create an actin stabilized strain, V159N, which
was discussed in the progress report. We plan to use this
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Bac2 Enzyme Lab Report
Title: BCAT2
Enzymes the most important role of enzyme is to increase the speed of reactions to the extend that some reactions are multiplied millions of times in
fraction of second. Another factor about enzymes is that they are not consumed in chemical reaction and much more they don't alter equilibrium of a
reaction .Enzymes can be seen in blood, gastric juices ,saliva, and fluids in the intestines. Enzymes also function as blood clotting. Branched Chain
Amino–acid Transaminase–2 (BCAT2) is an aminotransferase enzyme which uses О±–ketoglutarate in a big amount to form branched chain О±–keto
acids and glutamate. BCAT2 is found in mitochondrial inner membrane. The structure of BCAT in humans is consists of two parts: a small subunit and
large subunit which are tied by a short looping connecting region. Each unit consists of four alpha–helices and a beta–pleated sheet .The ties in humans
are all trans with the exlusion of bond between residues Gly338–Pro339. It ... Show more content on Helpwriting.net ...
These mice illustrate the best example model for studying BCAA metabolism and its toxicity. First, ENU treated mice were given a BCAA–restricted
diet after a while it was noticed that some symptom of human MSUD appear on them : decline in thrive,weakness,hair loss and weight loss. All these
symptoms in comparison with control group provide evidence that there was mutation that is liable to affect human beings as well. Sequencing of
branched–chain aminotransferase genes (Bcat) showed no mutation in the cytoplasmic isoform (Bcat–1) but instead display a homozygous splice site
mutation in the mitochondrial isoform (Bcat–2). The mutation caused a removal of exon 2, an obvious reduction in Bcat–2 mRNA, and a default in
pair BCAT–2 protein and its enzyme

Biology Exam Paper
FALL 2016
Gene Organization and Expression – 410.610.82
Exam I
Johns Hopkins University
Zanvyl Krieger School of Arts and Sciences
Advanced Academic Programs This exam is an open–book, open–note exam. You will have one week to complete the questions. You must submit
through the assignment in the Lesson. Late submissions will be penalized 10% for the first day and 20% each day after. Answer both questions on the
exam. You can use all resources available to you to research these questions, but your answers must be yours and yours alone.
Style: Pretend you are at the front of the class and I have asked you these questions. Imagine how you would say the answer out loud.
Do not quote! You can't memorize quotes; you're in front of the class.
Do not cite literature! This isn't a paper, it's an answer to a question I've asked you.
Each answer should fit in on a single page, single space or two page, double space using 12 pt. font (you may delete the question)!
Good Luck!
1. Compare the characteristics of ... Show more content on Helpwriting.net ...
The concept of protein domains and motifs has dominated the first half of this course. Discuss the relevance of protein domains to the following topics:
a)binding of proteins to DNA
Domains are parts of proteins that have some known structure and functionality. Therefore, DNA binding are stretches of a protein that contains some
known structural motif and has a high affinity for DNA allowing the two to bind.

One example of a proteins domain that binds DNA is the zinc finger which appear more than any other protein in eukaryotes. Zinc fingers are named
for their finger–like appearance and can bind not only zinc, iron and other metals but also DNA, RNA and others.
Another example is the leucine zipper which gets its name from the pattern–like occurrence of leucine throughout the protein's two О± helices. Leucine
zippers bind to promoters and induce transcription, ultimately expressing the gene.
b)binding of proteins to other

Strain Saccharomyces Cerevisiae Lab
Control of Uracil and Leucine Genetic Reproduction in the Strain Saccharomyces cerevisiae
Kristin S. Armstead
Rowan University Department of Biology
201 Mullica Hill Road
Glassboro NJ 08028
The purpose of this study was to obtain better and grasp on the genetic makeup of the strain of yeast being observed known as Saccharomyces
cerevisiae. The main objective of the study was to observe S. cerevisiae genetic capability to sustain itself in a nutrient deprived environment. More
specifically the focal point of the study were uracil and leucine: important component in yeast which are needed in order for yeast to grow. This
specific strain of yeast is good to work with due to its quick production rate, and easily changeable DNA. The ... Show more content on Helpwriting.net
...
cerevisiae were obtained and labeled accordingly. These served as the starting point for the experiment. An untainted YPD plate is retrieved and
sectioned into three areas and labeled: "A", "B", and "C". A small sample of each strain of yeast is taken and lightly spread onto its own section of
the YPD plate. The plate will then be left in the incubator at 30 В° C for 24 hours. In the time preceding time five more media plates are acquired
and labeled according to a key that indicates the type of media it is. After the time of incubation the original YPD plate is then replicated on
SD+His+Leu, SD+His+Ura, SD+His+Leu+Ura and YPD plates (YPD being the control). Each plate needs to be labeled in the same manner as the
first media plate so observations can be correctly made. Each replica place should also be labeled according to which strains are going to be
transferred to it. A cylinder shape block, with a compression ring is used along with a precut section of velvet in order to transfer an identical pattern
of the yeast on the original plate. All of the plates are reentered into the incubator for 48 hours, then the new growth is observed and

FLRT3 Lab Report
If PTC cells harboring mutations are found to be more mesenchymal than PTC cells containing mutations by having less E–cadherin and more
N–cadherin, then these results would suggest that FLRT3 drives papillary thyroid cancer progression as shown through increased EMT. However, if
differentiation of cadherin expression is observed for FTC cells harboring mutations in the presence or absence of FLRT3, then the results would
indicate that FLRT3 does not progress PTC specifically. In the resistance to apoptosis experiments, if the absence of FLRT3 in indicated PTC mutant
cell lines increases apoptosis when treated with apoptotic inducing agents, then the data would suggest that the PTC mutant cells are less resistant to
apoptosis in the... Show more content on Helpwriting.net ...
Our hypothesis that FLRT3 increases the binding affinity for FGF8 specific RTKs for PTC cells harboring mutations will be confirmed if the in vitro
binding assay displays an intense band for FGF8 specific RTKs in comparison to in vitro environments not containing FLRT3. However, if there
appears to be no difference, then it would appear that FLRT3 positively regulates FGF8 signaling not through protein–protein interactions. If leucine
rich domain deletions of FLRT3 decreases ERK phosphorylation in vivo, then it would appear that this specific domain is involved in increasing
MAPK activation. However, if there is no change in ERK phosphorylation in response to these truncations, then it would appear that FLRT3 does no
increase MAPK activation via leucine rich domains. As a result, I would investigate its role with fibronectin in progressing PTC. If a domain deletion
does appear to reduce ERK phosphorylation, then I would perform mutate specific leucine residues to glutamine in that indicated domain. I would then
infect PTC cells harboring mutations with the created leucine to glutamine mutated FLRT3 and immunoblot lysates for p–ERK in order to determine
the specific residues responsible for increasing MAPK activation. Overall, if FLRT3 expression does appear to show increased MAPK activation, then
it would be interesting to determine exactly how

The Chemical Structure Of Pregabalin
Introduction Pregabalin, trade name Lyrica, approved for its anticonvulsant properties and to relieve pain in those who suffer from diabetic neuropathy.
The chemical structure of pregabalin is structurally analogous to Оі–aminobutyric acid (GABA), an inhibitory neurotransmitter found in the central
nervous system and functions by binding to О±2Оґ voltage–gated calcium ion channel in presynaptic, inhibiting the release of neurotransmitters, most
notably GABA. By decreasing the amount of the inhibitory neurotransmitter GABA in synaptic terminals, epileptic seizures can be controlled and
prevented.1
Each drug displays its own properties when introduced to the body and all traits must be evaluated to observe effectiveness and side effects that may
occur. Pregabalin, although structurally and functionally similar to gabapentin (trade name Neurontin), has been shown to be more potent and exhibits
linear kinetic properties, unlike gabapentin. Some factors that contribute to its success are that it has a bioavailability of 90%, 98% is excreted in urine
unchanged, thus no or few side reactions occur, and it is able to pass through the blood–brain barrier. Beneficial effects of taking pregabalin can be
observed in as little as 2 days of administration, unlike most other central nervous system drugs, which typically take effect.1
Pregabalin is prescribed to treat conditions such as epilepsy and diabetic neuropathy. In addition, pregabalin has been approved for the treatment of

Protein Milk Proteins
Protein
Types of Protein Milk proteins are extensively studied regarding their role in exercise training adaptations (Hartman et al., 2007; Tang, Moore,
Kujbida, Tarnopolsky, & Phillips, 2009). Ingestion of milk proteins following exercise is shown to accelerate muscle recovery, increase glycogen
replenishment, and improve protein balance in a positive manner that allow for increases in muscular strength and hypertrophy (Cockburn, Stevenson,
Hayes, Robson–Ansley, & Howatson, 2010; Hartman et al., 2007; Tang et al., 2009; Wojcik, Walberg
–Rankin, Smith, & Gwazdauskas, 2001). Milk
proteins also contain the greatest amount of leucine compared to plant based counterparts (L E Norton & Wilson, 2009). There are two classes of milk
proteins, whey ... Show more content on Helpwriting.net ...
Thus suggesting that a fast–acting protein such as whey is a more appropriate protein source than casein when examining muscular adaptations in
regard to supplementation.
Protein and Leucine There are 20 specific amino acids that are utilized to build proteins utilized in tissue formation, cellular function, and growth (P. J.
Atherton & Smith, 2012; Fluck, 2012; Wu, 2009). Of these 20 there are essential (EAA) and non–essential (NEAA) based amino acids, those unable to
be synthesized and those able to be synthesized within the body respectively. Due to EAA's needing to be introduced via diet, any decreased
consumption of these amino acids would impair the body's ability to properly translate any cellular proteins (Fluck, 2012). Any increase in plasma or
myocellular amino acids above fasting levels promotes, while transient, an increase in protein synthesis, and reaches its peak roughly 2 hours following
ingestion which allows for muscle to be receptive to the anabolic effects of protein (Pasiakos & M., 2012). The ability for a protein to aid in muscle
mass accretion is largely based on its profile of EAAs. Animal based proteins are considered complete proteins as they contain all EAAs, while plant
based proteins lack certain EAAs making them incomplete. When consuming an isonitrogenous and isoenergetic serving of skim milk and soy milk
with 18 grams of protein, the skim milk was able to stimulate muscle protein synthesis to a greater extent, 0.1%

Chemical Origin And Impact Of Glut1 Deficiency Syndrome
Glucose Transporter–1 (GLUT1) Deficiency Syndrome is a relatively novel disorder. Studies highlighting the biological origin and impact of GLUT1
Deficiency have only recently been conducted, the disorder was first described by Dr. De Vivo in 1991 (Aktas et al., 2010; De Vivo, Leary, & Wang,
2002). Although rare, there have been studies conducted highlighting the causes and impact of the syndrome. Wilhelmina Leen, one of the authors of
An Analysis of Glucose Transporter 1, collected genetic data from fifty–seven different patients that suffer from GLUT–1 Deficiency Syndrome. Leen
as well as her co–authors work have opened new insights into better understanding the source as well as treatments for GLUT1 Deficiency syndrome.
However, to... Show more content on Helpwriting.net ...
An individual can be diagnosed with GLUT1 deficiency using multiple tools to deduce its presence. The primary testing for GLUT1 deficiency is
through measurement of glucose and lactate concentration in the cerebrospinal fluid. Low levels of glucose and lactate in the fluid indicate the onset
of the disease (Suls et al., 2009). Most of the phenotypic abnormalities can be treated or reduced utilizing a ketogenic diet. Since ketone bodies utilize a
different transporter to facilitate the movement of nutrients they can supply the brain with a viable fat–derived source of energy which ultimately can
reduce the onset of epilepsy (Leen et al., 2010).
Mutation Analysis
An analysis of fifty–seven patients with GLUT1 deficiency syndrome was conducted by Leen and associates and seventeen different missense
mutations of SLC2A1 were discovered. Of the seventeen mutations, a single nucleotide of adenine in the third helix domain of the SLC2A1 gene was
substituted with a guanine. This missense mutation found on the 286th base pair caused the codon to generate the amino acid valine rather than
methionine as seen on figure 2. This single missense mutation caused the classic phenotype expression of epilepsy in patient three, an 8–year–old
female child. Two other patients in the study had a mutation in the third helix in the transmembrane portion of theprotein, however their SLC2A1 gene
contained a deletion rather than a missense

P-Glycoprotein Inhibitor
P–glycoprotein Inhibitor Improvement: Verapamil
There are plenty of drugs that are targeting P–glycoprotein (p–gp), which is typically located in intestinal epithelial cells where drugs absorption
occurring. The p–gp controls in and out of most of foreign substrates from the blood stream. It contributes to balancing out the concentration of drugs in
the blood vain through reuptake process, especially efflux pump in this case. Therefore, this protein has been called as multidrug resistance because it is
able to excrete the drugs into the lumen. Accordingly, the p–gp inhibitor has an important role for the drug bioavailability and transportation. As the
p–gp inhibitor works in the vivo, the reuptake of drug will be decreasing which means decreasing the ... Show more content on Helpwriting.net ...
Keisuke Yusa and Takashi Tsuruo, AACR[online], 1989, 49, 5002– 5006
2.Manuel G., Lluis M. MIR, Stephane Orlowski, EJB, 1996, 244, 664 – 673
3.Sean Ekins, et al, ASPET[online], 2002, 61, 974 –

Protein Analysis
Proteins are an essential component of the human body tissues. They are made by combining amino acids together. There are many pros as well as
cons to consuming inadequate amounts of protein each day. Making sure to consume the accurate type and amount of protein is important for the body.
There are specific groups that do require more protein, however, if you are not a part of one of these groups consuming too much protein can have
harmful effects. Proteins are made when amino acids combine to each other. There are 20 different amino acids; 9 are essential amino acids and 11 are
non–essential amino acids. The body is unable to produce essential amino acids on its own. The body must obtain the 9 essential amino acids through
the consumption ... Show more content on Helpwriting.net ...
These groups include children, athletes, vegetarians, adolescents, and pregnant woman. Since proteins help with the growth of tissue in the body as
well as hormones and enzymes it is important for vegetarians as well as vegans to make sure they are consuming adequate amounts of protein. Animal
products contain the majority of sources for amino acids where many plant products are missing those sources that our bodies need. Dr. Hubbard
explains in the article "Are You Getting Enough Protein" published by Tufts University how animal products can provide the "complete proteins" but it
is possible to get them in other ways such as peanut butter, beans, rice, and bread. Dr. Hubbard states: "Despite what you may have heard, these
combinations don't have to be eaten at one meal– it's a balance over a whole day that's most important" ("Are You Getting Enough Protein," 2012).
Another group that needs to ensure that they have enough protein in their diet is athletes. According to a journal titled "Protein food and amino acid
supplements in athletes' diet," the amount of protein required over the daily recommended amount depends on the athlete as well as the sport. All
athletes can benefit when an extra supply of protein is consumed immediately following a workout in order to help increase muscle mass and strength
endurance. Protein consumption also helps athletes with recovery time and enhances their performance both in exercise and in a

Maple Syrup Urine Disease Research Paper
Maple syrup urine disease is a disease that effects 1 in 185,00 infants worldwide. It is an autosomal recessive disease which means both parents
would need to be either a carrier or have the disease, as seen in the graph from MedlinePlus at the bottom of the page. According to the (U.S.
National Library of Medicine,2017) the disease is caused by a mutation in the BCKDHA, BCKDHB, and DBT gene. Which in turn makes the body
lack an enzyme called BCKDC. Which is responsible for breaking down the amino acids leucine, isoleucine, and valine. These amino acids are in
many types of food most commonly found in protein–rich foods such as meat, milk, and eggs. Where if you eat those kinds of food your body will not
be able to break down those amino... Show more content on Helpwriting.net ...
Which are coma, feeding difficulties, lethargy, seizures, vomiting, and urine that smells like maple syrup. In the urine, there will be signs of ketones.
Ketones are the substances your body breaks down for energy. So, if it's in your urine that means that your body is not getting energy from it. There
will also be an excess acid in the blood. There are few treatments to this disease. Treatments involve eating a protein free diet, fluids and sugars can
also be given through an IV. You also might need dialysis through your belly and veins to clear out any abnormalities in your blood. With this
disease, you will need to constantly be on a very special diet. For infants, they need to be fed formula with low levels of leucine, isoleucine, and
valine. While adults should avoid foods with leucine, isoleucine, and valine. The reason why dieting does help lessen the symptoms is that if you
do not eat food with the affected amino acids then your body would not have the buildup of BCAAs and other substances which will cause health
problems. If you do not follow the diet and take precautions it can cause neurological damage. Even if you diet like you are supposed to you are still
susceptible to get the symptoms because high amount of stress and certain illnesses can cause high amount of amino acids in your body which your
body will not be able to break down. This can cause

Hydrophilic Coil Structure
The hydrophilic residues are located on the solvent accessible surface of the leucine zipper, enabling these residues to interact with the water in the
surrounding. This arrangement reduces the free–energy of protein folding by burying the hydrophobic residues in the interior of the protein, while
exposing the hydrophilic residues to the water containing environment and thereby, stabilizing the coiled–coil structure.
Q37. The О± helices of the leucine zipper motif can recognize and bind to DNA specifically, providing a scaffold for interaction of proteins with DNA.
Q38. The coiled coil structure contains approximately 3.5 residues per turn, with every seventh residue having an equivalent position as related to the
helix axis. In addition, the ... Show more content on Helpwriting.net ...
Yes. The DNA–binding residues are located within the zipper motif, at the basic regions of the helices.
Q41. There are several hydrogen bonds between the protein and the base pairs of the DNA such as the cytosine at position 34, cytosine at position 12,
and tyrosine at position 29. In addition, there seem to be several hydrogen bonds between the protein and the phosphate backbone of the DNA such as
the oxygen in the phosphate group at position 33.
Q42. The arginine–234 forms two hydrogen bonds with the phosphate backbone at position 27.
The arginine–241 forms three hydrogen bonds with the phosphate backbone at position 28.
The arginine–245 forms one hydrogen bonds with the phosphate backbone at position 29. The arginine–243 forms two hydrogen bonds with the
phosphate backbone at position 9. The arginine–232 forms one hydrogen bonds with the phosphate backbone at position 33. The arginine–240 forms
three hydrogen bonds with the phosphate backbone at position 32.
Q43. Yes. The asparagine that hydrogen bond with two contiguous base pairs at the center of each half–state is located at position 235.
Q44. Yes. The two alanine that make van der Waals contact with the thymine methyl group

Acne Vulgaris
While researching the western diet and its effect on acne vulgaris; one of the most common skin conditions found in teens and young adults, a strong
correlation between foods with a high glycemic index, foods high in fat, and dairy products have been discovered to have adverse effects of the
production of acne. The high glycemic index of foods such as pastas, breads, and cereals have been found to increase blood sugar rapidly and therefore
increase insulin production, subsequently causing acne causing hormones and cells to become alert and overactive. Similarly to foods with a high
glycemic index, meats with a high concentration of fat act similarly and active proteins such as leucine which overstimulate the production of keratin
and fluids

Inborn Errors Of Metabolism
Inborn Errors of Metabolism are group of rare disorders characterized by metabolic pathways abnormalities leading to underproduction of necessary
metabolites. One such disorder is Maple Syrup Urine Disease (MSUD) otherwise known as Branched–chain Ketoaciduria, a dangerous condition in
which over saturation of amino acids in the blood can lead to toxicity progressing to encephalopathy, neurodegeneration, coma or respiratory failure. the
etiology of the genetic disease, the mechanism of the genetic disease (if known) MSUD results from a malfunction of the branched–chain
alpha–ketoacid dehydrogenase complex (BCKD). This complex produces enzymes necessary for the proper breakdown of common amino acids such
as valine, leucine and isoleucine found... Show more content on Helpwriting.net ...
Some studies have found that the level of incidence for ashkenazi jews, Mennonite population and the amish is greater than in the average population.
(http://www.annclinlabsci.org/content/41/2/167.full) Detection of the disease is first identified via clinical symptomatology namely: smell of maple
syrup in the earwax about 12 hours after birth, irritability or difficulty feeding present two to three days after birth , movements resembling
"fencing" or "bicycling" present four to five days after birth, coma or respiratory failure by day seven or ten after birth. To diagnose the disorder
within the first couple of days urine could be tests of abnormally large amounts of ketones (day 3–4), the concentration of branched–chain amino acids
(BCAAs) and allo–isoleucine can be checked within the first day after the infant had an intake of protein. During BCAA testing leucine levels are
most important to note as they will be elevated in MSUD, while isoleucine and valine could be non–specific. Allo–isoleucine is the more definitive
indicator of MSUD. (http://www.ncbi.nlm.nih.gov/books/NBK1319/). An increase in leucine leads to a decreased in other amino acids such as:
tryptophan, histidine, glutamine, glutamate, alanine, tyrosine. Testing for the levels of these amino acids along with BCAAs could indicate that the
infant is

Cellucor Research Papers
There are loads of muscle building supplements out in the business today. Some help lose your muscles. Others help you get more fit also. Taking these
supplements are a portion of the wellness and sustenance day by day schedule that many bodybuilders take after regularly so that they can accomplish
a definitive nourishment and look that they need.
One of the names that is pretty famous in this industry or trade is Cellucor. Cellucor is an organization which produces and disseminates a gathering of
supplements that help with "weight reduction and muscle body building". Cellucor supplements help a lot in bodybuilding.
One specific package that the Cellucor Organization offers helps a man increase bulk in the compelling way. It's comprised of the supplements R3
Amazing, P6 Great and M5.
What is ... Show more content on Helpwriting.net ...
That is on account of they're made with ingredients that work together to increase your vitality and perseverance, expand quality, wrench up muscle
development, and burn off body fat.
A branched chain amino acid (BCAA) is an amino corrosive having aliphatic side–chains with a branch (a focal carbon molecule bound to three or
more carbon molecules). Among the proteinogenic amino acids, there are three BCAAs: leucine, isoleucine and valine. Non–proteinogenic BCAAs
incorporate norvaline and 2–aminoisobutyric acid.
The three proteinogenic BCAAs are among the nine key amino acids for people, representing 35% of the crucial amino acids in muscle proteins and
40% of the preformed amino acids needed by warm blooded animals.
Breaking down of bcaa
Degradation of cellucor bcaa includes the branched chain alpha–keto corrosive dehydrogenase complex (BCKDH). A lack of this complex prompts a
development of the branched chain amino acids (leucine, isoleucine, and valine) and their toxic by–items in the blood and urine, giving the condition
the name maple syrup urine

Maple Syrp Disease
Maple Syrup Urine Disease is a potently fatal disorder which affects the body's ability of breaking down three Branched chain amino acids: isoleucine,
leucine and valine. The inability of breaking down the three–branched amino acid chain is due to defect in an enzyme called branched chain alpha
ketoacid dehydrogenase. Which is the enzyme responsible for breaking down isoleucine, leucine and valine. This will result in high levels of the
branched amino acids in plasma and alpha ketoacid in urine. The presence of alpha ketoacid in urine will result in a burned maple syrup odder.
Hence the name, Maple syrup urine disease (MSUD). Maple Syrup disease is inherited in an autosomal recessive pattern. Both of the parents have to
be a carrier of the

Maple Syrup Urine Disease Analysis
160030
Maple Syrup Urine disease
Maple syrup urine disease (MSUD) is a rare genetic disorder characterized by deficiency of certain enzymes (branched–chain alpha–keto acid
dehydrogenase complex) required to break down (metabolize) specific amino acids in the body.(WebMD, 2015)
History
MSUD was first brought up by a pediatrician by John Menkes in 1954. He first noticed it by observing a family that happened to have several cases
of MSUD. In the study he had lost four babies within three months. Physicians and biochemists both worked as a pair to define this "inborn error of
metabolism." In history these problems in nature acted as a tool for investors as a genetic tool to tell us unknown pathways and why MSUD is used
as this role for BCAA(in ... Show more content on Helpwriting.net ...
The odor is caused when someone is not able to metabolize the branched chain a–ketoacid (BCKA). This problem happens because of their branch
chain amino acids (BCAA); leucine, isoleucine, and valine.
Other Problems Associated With Maple Syrup Urine Disease(Diet) Leucine is not a good acid to to have while having MSUD, but it is a necessary
amino acid that you need to have. It is the most toxic of the BCAA and it is in foods in higher percentages than valine or isoleucine. Every patient is
different so their tolerance of leucine has to be calculated to follow the measurement of BCAA levels. Then it has to be remeasured at the correct
intervals for the first six to 12 months. (Diet.com, 2004)
Risk Factors The National Organization for Rare Disorders (NORD) says that MSUD happens to males and females at the same rate. The risk of
having any form of MSUD depends if your parents have this disorder or not. If both of the parents have the disorder, each child has a 25 percent
chance of getting two mutated genes and getting MSUD, the child would have a 50 percent chance from getting one normal gene from each parent. The
parent or parents are not able to pass on the gene to their children if they have two normal genes for MSUD. (Healthline,

Factors Associated With An Autosomal Recessive Hereditary...
Discussion:
MSUD is a disorder of BCAAs metabolism with a frequency of 1/185,000 live newborns all over the world, while incidence is quite high in Eastern
part Pennsylvania as high as 1 in 200(1). It is an autosomal recessive hereditary metabolic disorder is due to defective oxidative decarboxylation of the
branched–chain alphaketoacids (BCKAs) derived from transamination of the the BCAAs, valine, leucine and isoleucine. The oxidative decarboxylation
of this BCKAs is catalyzed by the branched–chain alphaketoacid dehydrogenase (BCKDH) complex(2). These mutations sub classifies MSUD in
MSUD type 1 or MSUD type 2.Traditionally, the metabolic phenotype of MSUD is described classic or intermediate variety on related residual
BCKAD enzyme ... Show more content on Helpwriting.net ...
Because significant proximal tubular reabsorption of filtered BCAAs, renal clearance of filtered BCAAs very is limited and treatment of symptomatic
patients with MSUD aimed on reducing plasma BCAA levels either by incorporation into new protein synthesis or by enhancing removal from the
intravascular space. Several treatment modalities including special nutritional regimens, exchange transfusions, peritoneal dialysis, and continuous
hemofiltration have been utilized in neonates with MSUD. All this modalities has varying success in reducing systemic BCAA levels(6). MSUD is
very rare in most populations worldwide, published reports of diagnosis and treatment of MSUD usually involve only a few patients and most have
focused on management of the acute illness. As a result, reaching an agreement about various management issues has been difficult. In our case we
found continuous veno– venous hemodialysis with filtration (CVVHDF) as an effective treatment modalities which has been described in
earlier(7)(8)(9), as leucine level reduced to 20 % after 6 hours of treatment.
Acute metabolic crisis in MSUD treated effectively with use

Leucine-Rich Repeat Kinase 2 : An Analysis Of Parkinson's...
Leucine–Rich Repeat Kinase 2 is associated with several diseases, such as cancer, inflammatory bowel disease and multibacillary leprosy, but has its
clearest link with Parkinson's disease (Cogo, Greggio & Lewis, 2017). Up to now, several PD–associated autosomal dominant mutations in LRRK2
have been discovered, including G2019S, R1441C/G/H, Y1699C, I2020T and N1437H, indicated in figure 2. Of these mutations, which all entail
amino acid
Figure 3. Illustration of the protein secondary and tertiary structure of the kinase domain of the LRRK2 protein of a brown rat, consisting of both
О±–helices and ОІ–sheets, coloured coded from red at the N–terminus to blue at the C–terminus. Shown in 'sticks' format is the highly selective, potent
This suggests that both enzymatic structures are of critical value for maintaining normal physiological LRRK2 function. Mutation R1441C/G/H has
been shown to up–regulate kinase activity as well, suggesting that mutations that occur in the ROC domain also increase kinase activity (Li, Tan & Yu,
2014). MacLeod et al. (2006) have revealed by pathologically examining patients with LRRK2 mutations that degeneration of dopamine neurons in the
SN occurs. They showed mammalian LRRK2 plays an essential role in regulating neurite maintenance and neuronal survival, since mutant forms of
LRRK2 led to reduced neurone process length and complexity and ultimately apoptosis. Overexpression of both G2019S and I2020T resulted in a
dramatic neurite length reduction, as can clearly be seen in figure 4 (MacLeod et al., 2006). As a follow–up, Parisiadou et al. showed in 2009 that this
neuronal development was regulated by LRRK2 through modulation of ERM (ezrin, radixin and moesin) protein activity and actin polymerisation
(Parisiadou et al., 2009). They showed that over–expression of LRRK2 due to the G2019S mutation inhibited neurone outgrowth, increased
phosphorylation of ERM proteins and increased the content of F–actin, which is actin that is present in linear polymer microfilaments, in filopodia.
ERM proteins are, therefore, thought to be a physiological substrate of the kinase activity of LRRK2. It is this increased presence of ERM proteins
that plays a role in the developmental

Chapter 8 Microbial Genetics
Microbiology: An Introduction, 11e (Tortora/Case) Chapter 8 Microbial Genetics 8.1 Multiple Choice Questions 1) A gene is best defined as A) a
segment of DNA. B) three nucleotides that code for an amino acid. C) a sequence of nucleotides in DNA that codes for a functional product. D) a
sequence of nucleotides in RNA that codes for a functional product. E) a transcribed unit of DNA. Answer: C Skill: Recall 2) Which of the following
pairs is mismatched? A) DNA polymerase– makes a molecule of DNA from a DNA template B) RNA polymerase– makes a molecule of RNA from
an RNA template C) DNA ligase– joins segments of DNA D) transposase – insertion of DNA segments into DNA E) DNA gyrase– coils and twists
DNA Answer:... Show more content on Helpwriting.net ...
B) phosphate. C) deoxyribose. D) thymine. E) The answer cannot be determined based on the information provided. Answer: C Skill: Recall 21)
The damage caused by ultraviolet radiation is A) never repaired. B) repaired during transcription. C) repaired during translation. D) cut out and
replaced. E) repaired by DNA replication. Answer: D Skill: Recall Table 8.2 Codon on mRNA and corresponding amino acid |UUA |leucine |UAA
|nonsense | |GCA |alanine |AAU |sparagine | |AAG |lysine |UGC |cysteine | |GUU |valine |UCG, UCU |serine | 22) Refer to Table 8.2. If the sequence of
amino acids encoded by a strand of DNA is serine–alanine–lysine–leucine, what is the order of bases in the sense strand of DNA? A) 3'
UGUGCAAAGUUA B) 3' AGACGTTTCAAT C) 3' TCTCGTTTGTTA D) 5' TGTGCTTTCTTA E) 5' AGAGCTTTGAAT Answer: B Skill: Analysis
23) Refer to Table 8.2. If the sequence of amino acids encoded by a strand of DNA is serine–alanine–lysine–leucine, the coding for the antisense strand
of DNA is A) 5' ACAGTTTCAAT. B) 5' TCTGCAAAGTTA. C) 3' UGUGCAAAGUUA. D) 3' UCUCGAAAGUUA. E) 3' TCACGUUUCAAU.
Answer: B Skill: Analysis 24) Refer to Table 8.2 The anticodon for

The Actions of Heme-Group Containing Mammalian Peroxidase...
Heme–group containing mammalian peroxidase enzymes possess a highly conserved structure and partake in reactions associated with the
development of inflammatory diseases, defense system of the host as well as the biogenesis of hormones (PГ©terfi et al., 2009)(Cheng, Salerno, Cao,
Pagano, & Lambeth, 2008). The heme–binding sites of peroxidase enzymes possess specific features that are preserved as well as characteristics
including disulphide bonds forming between cysteine residues, a binding site for calcium as well as specific amino acid residues which interact with
the side chains present on the heme propionate (Chengreference). In the presence of hydrogen peroxide (H2O2), these enzymes catalyse the
oxidation of a range of substrates (PГ©terfi et al., 2009). In order to stabilise the extracellular matrix (ECM) of lower animal species as well as
plants, peroxidases enzymatically catalyse the cross linkage of these extracellular proteins through the formation of dityrosine bridges using H2O2
(PГ©terfi et al., 2009). The family of mammalian peroxidases consists of myeloperoxidase, eosinophil peroxidase and lactoperoxidase (which are
involved in the defense system of the host) as well as thyroid peroxidase (involved in the biogenesis of thyroid hormones) and the mammalian
peroxidasin (PXDN) (PГ©terfi et al., 2009).
The first form of peroxidasin was identified in Drosophila melanogaster and believed to have a role in the formation of the ECM during developmental
stages of the fly

What is Sarcopenia?
Sarcopenia is a degenerative disease frequently associated with the age–related loss of muscle mass and strength. Risk of sarcopenia increases at a rate
of 3–8% per decade after age 30 and continues to accelerate after the fifth decade of life (1, 616; 2, 1). Contributing factors of muscle degeneration
include: sedentary lifestyle, malnutrition, reduced protein turnover rate, lowered insulin response, inflammatory changes, and decreased anabolic
hormone production (3, 1073). Dietary protein is essential in order to build muscle and avoid loss of lean body mass (4, 686). Evidence indicates
increased protein intake above the RDA of 0.8 g/kg per day in older adults will increase the anabolic response of muscle (3, 1073).
High dietary protein ... Show more content on Helpwriting.net ...
A recent study observed the effects of amino acid infusion and results showed greater protein synthesis and no change in protein breakdown;
indicating increased amino acids are anabolic to muscle in healthy older adults (3, 1076). A moderate serving of a 113 gram serving of lean protein
containing 30 grams of amino acids and 10 grams of essential amino acids increases muscle protein synthesis by approximately 50% in the older adult
population (1, 621).
Leucine is an essential amino acid recognized as particularly important for signaling and muscle building (3, 1077). Leucine is activated through the
pathway of a kinase known as mTOR (3, 1078). Messenger ribonucleic acid translation, or mTOR, targets proteins involved in mRNA translation (3,
1078). Branched chain amino acid leucine with resistance exercise training is proposed to regenerates muscle and enhances anabolic pathways while
inhibiting catabolic pathways (2, 6). Leucine is a direct stimulate for muscle protein synthesis through increasing messenger ribonucleic acid
translation (3, 1077). Protein synthesis was fully restored when 46% leucine enriched bolus was distributed to a sample of older adults (2, 2).
Leucine at levels of 26% (1.72 g leucine) and 41% (2.79 g leucine) bolus increased muscle strength in the young but only the 41% bolus of leucine
essential amino acids was effective in older adults (1, 621). Leucine–enriched amino acids, with levels of leucine

Lysine And Protein Balance
influences our sleep, emotions, appetite, and sexual activity.
Threonine
Helps to maintain the proper protein balance in our body. It also is involved in the liver functioning, aids antibodies, and maintains the normal func–
tioning of our central nervous system.
Lysine
Lysine helps in the prevention of herpes infections and cold sores. It plays an essential role in growth, manages cholesterol levels, and absorbs calcium.
Valine
Valine is required for muscle repair, growth, andmetabolism. It regulates the nitrogen balance in the body and it also assists in the regulation of the
blood sugar and energy levels.
Histidine
This is essentially needed during periods of stress, growth, and recovery from illness and injury. Histidine

Non Polar Amino Acid Chromatography Paper
Hypothesis: If a polar amino acid is adsorbed by a polar matrix, then the polar matrix will not move as far along the matrix as a hydrophobic amino
acid. If this is so, the Rf value of a polar amino acid will be relatively small to that of a non–polar amino acid.
Introduction: In order to identify whether an amino acid is polar (hydrophilic) or non–polar (hydrophobic), the process of chromatography is used,
which separates the amino acids and identifies them based on specific chemical traits given by the R–groups. The process is preformed by placing
spots of the sample(s) on the origin of a matrix, or chromatography paper, letting it dry, then placing the edge of the paper with the samples on it into a
solvent (in this lab, it was alcohol).

Muscle Anaabolism
1 Introduction
Exercise has been repeatedly shown to have a strong relationship with intra–muscular protein metabolism. Muscular hypertrophy is only possible when
net anabolism occurs (Tipton et al., 2004). As a result, many athletes turn to supplementation to ensure there is positive protein balance in their diet to
increase the opportunity for hypertrophy and performance optimisation. Habitually athletic people have been shown to have a higher protein
requirements (Campbell et al., 2007),however the International Society of Sports Nutrition acknowledges that this higher requirement is possible to
achieve through a "balanced diet", it goes on to state that protein supplementation is also an practical way to ensure adequate protein intake (Campbell
(Tang et al., 2009) demonstrates a significant difference in muscle protein synthesis between casein and whey group, however (Wilborn et al., 2013)
found no significant difference in strength measures over 8 weeks. One would assume that if (Tang et al., 2009) results were extended over a 8 week
period, it would yield significant strength gain. (Tipton et al., 2004) goes some way to explaining this. The study demonstrates the short, intense nature
of whey protein on leucine concentration relative to casein, which was induced a significantly lower leucine concentration, however remained
significantly above the control group levels for longer than

Branched Chain Amino Acids Analysis
The Efficiency of Branched Chain Amino Acids (BCAAs)
Nowadays, it seems like every new supplement is the greatest at building muscle, improving performance or burning fat. With so many claims from
name brand supplement companies, it can be hard for individuals to weed out the good from the bad. In order to understand if a supplement is right for
you, you need to remember what the point of supplementation is.
Why do we need supplements?
The point of supplementation is to obtain a nutrient that your body is not receiving or not receiving sufficient amounts through diet alone. In this
article, we'll discuss whether BCAA's are something you need to incorporate into your diet, or if you're just pissing away your money. Literally.
What are Branched Chain Amino Acids?
First off, let's review what Branched Chain Amino Acids are (BCAA's for short). BCAA's are a combination of three specific amino acids that our
bodies cannot produce. These amino acids; leucine, isoleucine, and valine are found abundantly in animal products ... Show more content on
Helpwriting.net ...
But as far us gym rats, we probably won't see any benefit. In terms of reducing muscle soreness, BCAAs have been proven beneficial. But remember,
these studies used just BCAA supplementation alone. Most Whey protein shakes will contain these same levels of BCAAs, so additionally BCAA
supplementation may not be necessary. Lastly, those who have dietary restrictions from animal based products could see the biggest impact from
BCAA supplementation, as BCAAs are found scarce in the plant–based protein category.
At the end of the day, whenever you're looking into trying out a new supplement, do your homework. Research peer reviewed articles and studies about
the supplement, and compare the results with your own training goals. Supplements like BCAAs can help, but the greatest supplement of all is the
blood, sweat and tears you put into your training

The Effects Of Nutritional Supplementation On Improving...
The clinical study done by J. Bauer MD, PhD, S. Verlaan Msc, I. Bautmans, and others was done to address the loss of muscle strength, mass, and
physical performance correlated with age. The researchers wanted to test the effects of nutritional supplementation on improving mobility and
muscular confinement by reducing the effects of sarcopenia. Sarcopenia is described as the loss of muscular strength, mobility, and tissue due to
aging.(Mostly found in elderly people) When aging people experience sarcopenia, they will start to lose the ability to do tasks that require endurance
and strength, which leads to the need for assisted care. Also when elderly/aging people start to lose muscle mass and strength they will be prone to an
increased risk of injury. Ingesting supplements such as essential vitamins and amino acids are fundamentally important in reducing the severity of
sarcopenia. If the proper amount of nutrients are not taken it may lead to an increase in the onset of sarcopenia which increases risk factors for overall
health when aging. The researchers hypothesize that providing a targeted nutritional supplement containing whey protein enriched with leucine (~1.2g
/kg BW/day) and vitamin D in a timely amount would result in the muscular and physical improvements independent of physical exercise. (Bauer et al.
741)
The trial for this experiment would last approximately 13 weeks and would be controlled, randomized, and double–blinded. The participants were

Pulse Chase Experiment
What is the purpose of a Pulse Chase Experiment? The purpose obtain a half life on a molecule. A Half life is the amount of time it takes to get to
one half of a molecule. However, In Pulse Chase you can use proteins or mRNA which proteins it uses thirty–five S Met in the pulse and Met in the
chase. The quantity is immunoprecipitate and scintillation counting. In mRNA it ues three UTP in thePulse and UTP IN the Chase. The quantity is
affinity purify or dot blot and scintillation counting. So the method begins with the Pulse. Which is radiolabel newly synthesized molecules making
them hot. The Chase is making a new molecules not radiolabeled cold, Then we ask the question how many of the originally labeled hot molecules
are around at any given time? Over the course, of a Pulse Chase the total number of molecules does not change. The only thing that does is the ratio of
hot and cold molecules. The two thing that factor in is how fast can molecules produced, and how fast hot molecules can degraded. ... Show more
content on Helpwriting.net ...
But before it begins proteins molecules are being synthesized at a steady state trough a translation of mRNA by ribosome. The phase of the
experiment begins when investigators apply a large dose of a radioactive amino acid or leucine to the cell culture. The radioactive amino are
incorporated in the proteins manufactured during protein synthesis. The chase phase of the experiment begins when a very large amount of
nonradioactive leucine is added to the simple. After the chase beings no more radioactive proteins is made. The experiment results in a short period of
production of radiolabeled molecules. Which can be tracked within the

Branched Chain Amino Acid Research Paper
Branched–chain amino acids help decrease exercise–induced muscle damage, increase muscle recovery and regulate protein synthesis. They are also
very essential in reducing fatigue. This means that you will be able to train at a higher intensity for a prolonged period.
The BCAA refer to a group of important amino acids which include leucine, isoleucine, and valine. Though amino acids are the main building blocks of
protein, which the body cannot produce. So the BCAA amino acids must consumed as part of the daily diet.
Nearly all the proteins are made from the BCAAs. Researchers show that the BCAA'S are mainly leucine and handle regulating protein synthesis.
When are you supposed to use BCAA amino acids?
The branded chain amino acids are most beneficial when included with post–exercise recovery nutrition, ... Show more content on Helpwriting.net ...
For your post exercise recovery, ensure that you take adequate levels of BCAAs which is average must be 15 grams. The amount of leucine needed to
stimulate protein synthesis and improve muscle recovery is around 3,000 mg after heavy workout.
What you are supposed to know about the BCAA amino acids is that it can stimulate protein synthesis. The BCAAs may also play a role in delaying
central fatigue. When you ingest branched chain you increase the amount in the bloodstream, helps in balancing the free tryptophan associated with the
exercise. The amino acids decrease the amount of tryptophan transported to the brain, ultimately delaying fatigue.
There are a lot of benefits which are associated with consuming BCAAs during the various types of exercise. Some of these training include strength
training, endurance training, and general exercise.
As it can be seen from the research, the amino acids are very important supplements which must be included in the diet. As an athlete or any other
person who is looking to maintain the muscle or build up the muscles, you must have the branded chain amino acids as the main

The Infection Of Cattle And Dogs
The genus Babesia is composed of tick–borne intraerythrocytic apicomplexan protozoans that cause babesiosis in mammals, including humans
(Schnittger et al., 2012). The infection of cattle with Babesia bovis causes massive economic losses in the livestock industry worldwide (Bock et al.,
2004; Malak et al., 2012).
Similarly, Babesia gibsoni infects dogs worldwide, causing serious concern among pet owners with regard to animal health and welfare (Trotta et al.,
2009; Yeagley et al., 2009). Cattle and dogs clinically infected with B. bovis and B. gibsoni manifest fever, anemia jaundice, hemoglobinuria,
hypertensive shock, and more often deaths if left untreated (Bock et al., 2004). Due to the limited range of anti–Babesia drugs available, the treatment
of babesiosis is becoming increasingly difficult, particularly in areas where the disease is endemic (Gohil et al., 2012; Lin et al., 2012). Therefore, it
is clear that alternative strategies are required for the discovery and development of the much needed anti–Babesia drugs.
The M17 leucine aminopeptidases of Plasmodium falciparum
(PfM17LAP) and Plasmodium vivax (PvM17LAP) have been characterized and validated as a drug target (Cunningham et al.,
2008; Lee et al., 2010). The malaria parasite, just like Babesia species, destroys erythrocytes, causing many of the clinical symptoms responsible for the
disease. The PfM17LAP is involved in host cell hemoglobin digestion, metabolic regulation, intracellular housekeeping, and antigen

The Clinical Study Done By J. Bauer
The clinical study done by J. Bauer, S. Verlaan, I. Bautmans, and others was done to address the loss of muscle strength, mass, and physical
performance correlated with age. The researchers wanted to test the effects of nutritional supplementation on improving mobility and muscular
confinement by reducing the effects of sarcopenia. Sarcopenia is described as the loss of muscular strength, mobility, and tissue due to aging (Mostly
found in elderly people). When aging, people experience sarcopenia, they will start to lose the ability to do tasks that require endurance and strength,
which leads to the need for assisted care. Also, when elderly/aging people start to lose muscle mass and strength they will be prone to an increased risk
of injury. Ingesting supplements such as essential vitamins and amino acids are fundamentally important in reducing the severity of sarcopenia. If the
proper number of nutrients are not taken it may lead to an increase in the onset of sarcopenia which increases risk factors for overall health when aging.
The researchers hypothesize that providing a targeted nutritional supplement containing whey protein enriched with leucine (~1.2g/kg BW/day) and
vitamin D in a timely amount would result in the muscular and physical improvements independent of physical exercise. (Bauer et al. 741)
The trial of this experiment would last approximately 13 weeks and would be controlled, randomized, and double–blinded. The participants were
recruited from

Essay on Branched Chain Amino Acids On Sports Performance
With sportsmen seeking alternatives to illegal and unsafe performance enhancing drugs, "ergogenic aids" have come to their rescue. Ergogenic aids are
supplements that enhance the performance of athletes by improving their speed, strength and agility. A number of natural products are marketed as
ergogenic aids, which have found a ready market among sportspersons. Their biggest advantage is that they are legal, apart from being safe and
effective. Examples of such aids include branched chain amino acids, creatine, medium chain triglycerides, pyruvates and vitamins.
I. What are Branched chain amino acids?
Branched chain amino acids (BCAA) are amino ... Show more content on Helpwriting.net ...
Oxidation of these amino acids occurs in skeletal muscles. Though BCAAs are not used as a source of energy in the body under normal conditions,
they do contribute to energy generation during heavy and strenuous exercise. The subsequent breakdown of these amino acids for energy generation
during heavy exercise leads to muscle damage and tear. Therefore, restoring them with the help ofprotein supplements is extremely necessary to make
up for the loss of proteins.
IV. Effect on athletic performance Innumerable studies have investigated the effects of BCAAs on the performance of athletes. Studies and clinical
trials have investigated their potential role in decreasing fatigue, improving physical performance, increasing strength and affecting cognitive abilities.
A few of the most significant studies are discussed here. While BCAAs have been found to be of help in enhancing sports performance, there is lack
of sufficient evidence from clinical trials. Therefore, while the intake of BCAAs has been proved to be of help in some cases, their overall benefit in
enhancement of sports performance is still debated and needs strong evidence.
Reduction of fatigue
BCAAs are reported to reduce central fatigue

Maple Syrure Research Paper
Have you ever had maple syrup? Could you imagine having urine that looked like maple syrup? Maple Syrup Urine is a genetic disorder. What
symptoms happens to the body is that Maple Syrup Urine is a disorder in which the body can't break down certain parts of protein. The urine can
smell like maple syrup. This disorder is passed through families, and "is caused by a defect in 1 of 3 gene." (medlineplus.gov). "This disorder can't
break down the amino acids,leucine,isoleucine, and valine".(medlineplus.gov). It is also a build up of these chemicals in the blood. Most severe form
can damage the brain during times of stress (infection, fever, or not eating for a long period of time.) Some side effects of this are coma, feeding
difficulties, lethargy, ... Show more content on Helpwriting.net ...
How common is it?
This disorder affects one out of every 185,000 babies born worldwide. Also it is found in many countries throughout the world, although the condition
is more common in certain ethnic groups. "About one out of every 380 babies from the old order mennonite population is affected by the condition.
French– Canadian ancestry and Ashkenazi Jewish ancestry." (babyfirsttest.org) "In Maple Syrup Urine Disorder the group of enzymes called
branched–chain ketoacid dehydrogenase (BCKAD) complex is not working correctly. BCKAD is a group of four enzymes that work together to break
down the amino acid leucine."

Melittin Lab Report
The above structure is melittin, which, as discussed earlier, has lytic properties when it encounters several types of membranes. Experiments in
selectivity have been done with two different analogues of melittin that were produced, one in which the leucine at position 13 was replaced by
alanine, and one in which the 6th and 13th leucine residues were replaced by alanine. The first analog exhibited 10–20% of the hemolytic activity and
similar antimicrobial activity when compared to melittin, while the second analog showed 1–2% of the hemolytic activity and similar microbial
activity. These results indicate that the leucine zwitter–motif is responsible for the hemolytic, but not the antimicrobial, activity of melittin. (Asthana,
p.2)
Additional ... Show more content on Helpwriting.net ...
Peptides of the innate immune system have a broad range of microbicidal activities and can affect Gram positive and Gram negative bacteria as well as
mycobacteria, spirochetes, fungi, and some enveloped bacteria. The same can be said of magainin–2 and melittin.(Mark, 601)
Despite the wide–range of microbes affected by the innate immune system, the activity of peptides associated with the immune response seem to be
highly sequence specific. The peptides specifically target areas of the membrane with high curvature. (Mark, 601)
This examination of peptides found in the innate immune system, when combined with the research done involving analogs of melittin, lends some
hope that if pathogenic cell membranes can be mapped, then melittin can be altered in such a way as to target these cells. When compared to the
magainin–2 "all or nothing" response, melittin's graded response provides a window where certain concentrations that could be toxic to target cells are
still safe for host cells. This is why there is much research currently being done on melittin and its ability to target the HIV

Branched Chain Amino Acid As A Supplement For Long...
Branched Chain Amino Acid as a Supplement for Long Duration Exercise
Introduction
Branched Chain Amino Acids (BCAAs) are composed of three essential amino acids including leucine, isoleucine, and valine. They are unique in that
they are predominantly metabolized outside of the liver in the skeletal muscle. BCAAs make up 35–40% of the amino acid pool in the body and exist
in high concentrations in skeletal muscle tissue (Shimomura et al, 2006). While the supplemental dosage is dependent upon on the type of exercise,,
body composition, and dietary intake, a standard dosage of the combination of BCAAs is 20g, of leucine, isoleucine, and valine. Other ratio
combinations are available as well as individual supplement products of leucine and isoleucine. BCAA supplementation is often taken before, during,
and after exercise. It has been observed that BCAAs potentiate the effects of exercise by their anabolic processes on protein metabolism by increasing
the rate of muscle protein synthesis and decreasing the rate of muscle protein breakdown (Karlsson et al., 2004). Moreover, it has been theorized that
BCAAs may improve performance, reduce muscle fatigue, and feelings of muscle soreness.
Review of Literature
Various studies have demonstrated that BCAAs promote activation of protein synthesis, reduced muscle degradation, and reduce perceived feelings of
muscle fatigue. All human studies reviewed used randomized, double blind, within subjects cross–over design conducted

Bcaa Supplements
Supplements can help you not only get needed nutrients but also stay fit and in shape. However, it is important to take supplements at the right time
and in the right concentrations in order to derive the greatest possible benefit from them. Following is an overview of why you need pre– and
post–workout supplements as well as a detailed look at the highly effective BCAA capsules that are now widely available for purchase.
Pre–Workout Supplements
Taking supplements before you start working out will give your body the strength and nutrition it needs in order to engage in an effective workout
session. Experts recommend that supplements be taken anywhere from 15 to 45 minutes before you work out. You may also want to consider eating a
pre–workout meal an hour or two before you begin exercising. Taking the right ... Show more content on Helpwriting.net ...
These can either be consumed with a small meal or on their own. Supplements can be taken either right after you finish working out or an hour or so
later.
Introducing BCAA
BCAA stands for Branched–Chained Amino Acid and consists of three important amino acids: leucine, isoleucine and valine. Research clearly shows
that BCAA improves your energy levels, burns fat and builds muscle. This valuable supplement is available in drink form but tastes horrible, so those
who don't want to torture themselves right after a heavy–duty workout will probably want to take BCAA capsules instead.
What's the Best Ratio?
Leucine is commonly regarded as being the most important amino acid in the BCAA supplement combination. For this reason, some BCAA
supplements contain an 8:1:1 or even 10:1:1 ratio of leucine to other amino acids. However, it is important to note that a higher leucine content does
not necessarily boost muscle growth better than supplements with a low–leucine–to–other–amino–acid ratio. In fact, one study shows that the BCAA
capsules that were most effective were the ones with a mere 2:1:1

What Are Branched Chain Amino Acids?
Build Awesome Muscles with Branched Chain Amino Acids.
What are Branched Chain Amino Acids?
Branched Chain Amino Acids, also known as BCAAs, is a group of 3 specific amino acids. BCAAs can promote the production of muscle protein, help
increase muscle mass, minimize muscle loss, and prevent fatigue, allowing you to have a much harder workout.
BCAAs are essential nutrients which are obtained from the food we eat, especially meat, dairy products and legumes. The name Branched Chain
actually refers to the chemical structure of these particular amino acids, which differs from the structure of the other 20 or so amino acids the body
uses to form proteins.
The three types of BCAAs.
The three types of BCAAs are Leucine, Oleucine, and Valine. Each has a specific function which includes the ability to promote the production of
muscle–building protein in the body.
Leucine. This amino acid is unique in its ability to promote protein production in the skeletal muscle system. It is more anabolic in nature than other
amino acids, which means it is a potent builder of muscle and protein synthesiser.
Oleucine. Though weaker than Leucine, it is also able to promote the formation of protein in the cells and muscles. However its claim to fame is that it
increases the absorption and usage of glucose during exercise, which is converted into energy.
Valine promotes muscle growth and tissue repair. It also helps prevent muscle break–down by supplying the muscles with extra glucose for energy

Fatty Acid: A Catabolic Pathway
De novo lipogenesis comes to mind when thinking of the process of synthesizing fatty acids. This process can be described as the pathway in the body
to converting dietary intake to form fatty acids from Acetyl–CoA, or carbohydrate consumption. De Novo Lipogenesis slows and decreased when in an
insulin resistant system (1 Sanders). Insulin acts as a hormonal control of de novo lipogenesis. Acetyl–CoA must make its way to Malonyl CoA to
become fatty acid. If this regulated metabolic pathway is increased, it has a correlation to excess fat. Insulin can be found in the equation with de novo
lipogenesis, because DNL can take a pathway to the liver and to adipose tissues. Insulin and glucagon effect sterol regulatory element–binding proteins
like ... Show more content on Helpwriting.net ...
Cortisol, which is brought up with stress, is a catabolic hormone released from adrenal cortex. Cortisol can cause break down of muscle and atrophy
by not allowing amino acid metabolism to occur in muscles, or accelerating protein degradation through increasing activity of proteolytic caplain (16
Pandurangan). This causes lower lean muscle mass while raising fat mass. Since amino acids are not getting into muscle, there is an abundance of
amino acids which can be used for gluconeogenesis.Branched–chain amino acids can be metabolized for energy. –ketoglutarate help remove the amino
acid groups from valine, leucine and isoleucine to make branched–chain keto acids along with glutamate (3 Tiidus pg 191). Branch–chain keto acid
dehydrogenase is use to prevent the over buildup up of branch–chain amino acids (17 Harris). This process is the rate–limiting enzyme in the catabolic
branch–chain amino acid oxidation (18 Shimomura). Branched–chain ketoacid oxidation can be effected by changes in alanine, glutamine and
–ketoglutarate branch–chain amino acids quantities. Increased levels of alanine will be produced in conjunction with an increase BCAA oxidation.
This means during sustained periods of branch–chain amino acid oxidation, increased alanine is taken to liver for gluconeogenesis through the glucose
alanine cycle (19 O'Connell). When the body undergoes a hypocaloric state for a sustained period of time, the body tries to hold onto nutrients to
conserve for later energy. Instead of using up all the amino acids in muscles, amino acids such as alanine are taken to kidney for gluconeogenesis.
After more time free amino acids and ketone bodies become the bodies main fuel source. These stores can be lost through the urine, so to prevent loss
the kidneys hold onto these ketone bodies stores to help humans survive long periods of time in sustained

FLRT3 Case Study
We will evaluate if FLRT3 increases MAPK activation for normal thyroid cells, PTC cell lines harboring mutations, and FTC cell lines containing in
the presence or absence of FLRT3 treated or not treated with ectopic expression of FLRT3 via western blot analysis for p–ERK. We will quantify
FLRT3's effect on MAPK activation by using qPCR for c–fos and c–jun for indicated PTC mutant cell lines with or without FLRT3 in order to
compare the relative expression of these downstream MAPK response genes. To assess if FLRT3 increases the binding affinity of FGF8 for RTKs,
we will perform a binding assay using varying treatment times of GST–FGF8 followed by a GST–pull down and subsequent western blot for PTC cells
harboring mutations with or... Show more content on Helpwriting.net ...
Resistance to apoptosis will be assayed via western blot for Thyroid, FTC cells with mutations, and PTC with mutations treated and not treated with
siFLRT3 knockouts with antibodies specific for caspase–3 , actin and FLRT3. The appearance of caspase–3 indicates DNA damage and subsequent
apoptosis, since caspase is a DNA repairing protein that is cleaved when cells undergo apoptosis. Additionally, resistance to apoptosis will be calculated
using a TUNEL–assay protocol [4] for FTC cells harboring mutations, and PTC cells containing mutations treated and not treated with siFLRT3 and
infrared radiation. TUNEL assays quantify apoptosis by using TdT enzymes to bind to the 3' end of DNA in order to gauge the amount of DNA
fragmentation, a marker of apoptosis. We will evaluate FLRT3's impact on motility for FTC cell lines with / mutations by testing for metastasis over
various time intervals. Metastasis in vivo experiments will be performed by injecting immunodeficient mice in the tail with PTC cells containing either
or / mutations and checking for metastasis to the lymph nodes at various time intervals[5]. PTC cells with / / mutations will be generated by performing
a mouse knock out by isolating embryonic stem cells from / containing white mouse blastocysts and subsequently introducing в€†flrt3::neoR containing
plasmids with homologous primers attached into the cells

##S And How Deletion Of Ykl Affects The Processes

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##S And How Deletion Of Ykl Affects The Processes